Results 11 to 20 of about 9,257 (139)

The flavonoid galangin inhibits the L1 metallo-β-lactamase fromStenotrophomonas maltophilia [PDF]

FEMS Microbiology Letters, 2002
The flavonoid galangin inhibits the partially purified metallo-beta-lactamase from Stenotrophomonas maltophilia. The effect was not reversed by the addition of ZnCl(2) suggesting that the inhibitory effect is not related to metal chelation. The flavonoid quercetin also has some inhibitory effect against the enzyme.
Brian J, Denny, Peter A, Lambert, Patrick W J, West   +2 more
openaire   +2 more sources

Identification and characterization of a novel metallo β-lactamase, SZM-1, in Shenzhen Bay, South China

Frontiers in Microbiology, 2022
Metallo β-Lactamases (MBLs) degrade most clinical β-lactam antibiotics, especially Carbapenem, posing a huge threat to global health. Studies on environmental MBLs are important for risk assessment of the MBLs transmission among connected habitats, and ...
Lingxu Fang, Zongbao Liu, Zhongyi Lu, Zhongyi Lu, Rongzhong Huang, Rong Xiang   +5 more
doaj   +1 more source

Isolation and partial purification of a carbapenem-hydrolysing metallo-β-lactamase fromPseudomonas cepacia [PDF]

FEMS Microbiology Letters, 1994
A metallo-beta-lactamase has been isolated from a clinical strain of Pseudomonas cepacia and partially purified using Cibacron blue F3GA coupled agarose. The resulting preparation showed a single band of beta-lactamase activity (pI 8.45) after analytical isoelectric focusing.
I A, Baxter, P A, Lambert
openaire   +2 more sources

Inhibition of IMP-1 metallo-β-lactamase and sensitization of IMP-1-producing bacteria by thioester derivatives [PDF]

FEMS Microbiology Letters, 1999
IMP-1 metallo-beta-lactamase is a transferable carbapenem-hydrolyzing enzyme found in some clinical isolates of Pseudomonas aeruginosa, Serratia marcescens and Klebsiella pneumoniae. Bacteria that express IMP-1 show significantly reduced sensitivity to carbapenems and other beta-lactam antibiotics.
G G, Hammond, J L, Huber, M L, Greenlee, J B, Laub, K, Young, L L, Silver, J M, Balkovec, K D, Pryor, J K, Wu, B, Leiting, D L, Pompliano, J H, Toney   +11 more
openaire   +2 more sources

Cefiderocol: An Overview of Its in-vitro and in-vivo Activity and Underlying Resistant Mechanisms

Frontiers in Medicine, 2021
Treatment of multidrug-resistant (MDR) Gram-negative bacteria (GNB) infections has led to a global public health challenging due to the bacterial resistance and limited choices of antibiotics.
Jiahui Yao, Jin Wang, Mengli Chen, Yun Cai   +3 more
doaj   +1 more source

Characterization of the active-site residues asparagine 167 and lysine 161 of the IMP-1 metallo β-lactamase [PDF]

FEMS Microbiology Letters, 2001
The roles of lysine at position 161 and asparagine at position 167 in IMP-1 metallo beta-lactamase were studied by site-directed mutagenesis. These residues are highly conserved in metallo beta-lactamases and are thought to be present in the active-site cavity.
S, Haruta, E T, Yamamoto, Y, Eriguchi, T, Sawai   +3 more
openaire   +2 more sources

Time-resolved β-lactam cleavage by L1 metallo-β-lactamase

Nature Communications, 2022
Metallo-β-lactamases cleave β-lactam moiety of many broadly used antibiotics. Here the authors captured mechanistic details of the enzyme catalyzed reaction using time-resolved xray synchrotron serial crystallography.
M. Wilamowski, D. A. Sherrell, Y. Kim, A. Lavens, R. W. Henning, K. Lazarski, A. Shigemoto, M. Endres, N. Maltseva, G. Babnigg, S. C. Burdette, V. Srajer, A. Joachimiak   +12 more
doaj   +1 more source

Novel IMP-1 metallo-β-lactamase inhibitors can reverse meropenem resistance inEscherichia coliexpressing IMP-1 [PDF]

FEMS Microbiology Letters, 2005
IMP-1 metallo-beta-lactamase is a zinc metalloenzyme that confers antibiotic resistance to bacteria through the hydrolysis of beta-lactam antibiotics. Pathogens that express the enzyme show reduced susceptibility to carbapenems, such as meropenem and imipenem.
Joseph G, Moloughney, Janice, D Thomas, Jeffrey H, Toney   +2 more
openaire   +2 more sources

Occurrence of a new metallo-β-lactamase IMP-4 carried on a conjugative plasmid inCitrobacter youngaefrom the People's Republic of China [PDF]

FEMS Microbiology Letters, 2001
During the course of an antimicrobial resistance surveillance programme in Guangzhou, the People's Republic of China, single strains of Citrobacter youngae and Pseudomonas aeruginosa were identified which were resistant to imipenem and found to carry the carbapenemase gene bla(IMP).
P M, Hawkey, J, Xiong, H, Ye, H, Li, F H, M'Zali   +4 more
openaire   +2 more sources

Identification of 76 novel B1 metallo-β-lactamases through large-scale screening of genomic and metagenomic data

Microbiome, 2017
Background Metallo-β-lactamases are bacterial enzymes that provide resistance to carbapenems, the most potent class of antibiotics. These enzymes are commonly encoded on mobile genetic elements, which, together with their broad substrate spectrum and ...
Fanny Berglund, Nachiket P. Marathe, Tobias Österlund, Johan Bengtsson-Palme, Stathis Kotsakis, Carl-Fredrik Flach, D G Joakim Larsson, Erik Kristiansson   +7 more
doaj   +1 more source